scPDB - 4ge9 entry

Protein Data Bank Entry:

PDB ID : 4ge9

Resolution :2.430 Å

Experimental Method : X-ray

Deposition Date : 2012-08-01

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial
ID:	AADAT_HUMAN
AC:	Q8N5Z0
Organism:	Homo sapiens
Reign:	Eukaryota
TaxID:	9606
EC Number:	2.6.1.39

Chains:

Chain Name:	Percentage of Residues within binding site
A	35 %
B	65 %

Ligand binding site composition:

B-Factor:	24.900
Number of residues:	51
Including
Standard Amino Acids:	49
Non Standard Amino Acids:	0
Water Molecules:	2
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.844	752.625

% Hydrophobic	% Polar
48.43	51.57
According to VolSite

Ligand :

HET Code:	0L0
Formula:	C25H23N3O8P
Molecular weight:	524.439 g/mol
DrugBank ID:	-
Buried Surface Area:	79.73 %
Polar Surface area:	179.98 Å2

Number of
H-Bond Acceptors:	10
H-Bond Donors:	2
Rings:	4
Aromatic rings:	3
Anionic atoms:	3
Cationic atoms:	0
Rule of Five Violation:	2
Rotatable Bonds:	9

Mass center Coordinates

X	Y	Z
27.8356	18.4438	-52.1526

Binding mode :

What is Poseview ?

2D View
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Image generated by PoseView

Protein

Binding Site

Ligand

Interaction pattern

hydrophobic (CA)

aromatic (CZ)

hydrogen bond acceptor (O)

hydrogen bond acceptor/donor (OG)

hydrogen bond donor (N)

positively ionized (NZ)

negatively ionized (OD1)

metal (ZN)

Legend:

Represent the protein/ligand binding mode, centered on the ligand
Dashed lines represents hydrogen bonds and metal interactions
Green residue labels for amino acids with hydrophobic contacts (green lines) to the ligand

Image generated using PoseView by BioSolveIT

Ligand	Protein		Interaction
Atom	Atom	Residue	Distance (Å)	Angle (°)	Type
C25	CG2	ILE- 19	3.87	0	Hydrophobic	false
O18	NE	ARG- 20	3.49	164.7	H-Bond (Protein Donor)	false
C14	CD	ARG- 20	3.44	0	Hydrophobic	false
C15	CD	ARG- 20	3.36	0	Hydrophobic	false
C19	CG2	THR- 23	3.55	0	Hydrophobic	false
C19	CD2	LEU- 40	3.64	0	Hydrophobic	false
C22	CD2	LEU- 40	3.78	0	Hydrophobic	false
O48	OH	TYR- 74	2.57	165.41	H-Bond (Protein Donor)	false
C24	CE2	TYR- 74	3.22	0	Hydrophobic	false
C11	CG	TYR- 74	3.28	0	Hydrophobic	false
C17	CB	TYR- 74	4.25	0	Hydrophobic	false
C15	CB	SER- 77	4.44	0	Hydrophobic	false
O49	N	SER- 117	2.75	161.06	H-Bond (Protein Donor)	false
O49	OG	SER- 117	3.42	130.86	H-Bond (Protein Donor)	false
C8	CB	GLN- 118	4.3	0	Hydrophobic	false
O50	N	GLN- 118	3.16	161.33	H-Bond (Protein Donor)	false
C33	CE2	TYR- 142	4.14	0	Hydrophobic	false
C7	CB	TYR- 142	3.89	0	Hydrophobic	false
C8	CZ	TYR- 142	3.97	0	Hydrophobic	false
DuAr	DuAr	TYR- 142	3.67	0	Aromatic Face/Face	false
C7	CG2	VAL- 197	3.68	0	Hydrophobic	false
C7	CB	ASN- 202	4.11	0	Hydrophobic	false
O9	ND2	ASN- 202	2.83	151.87	H-Bond (Protein Donor)	false
O45	ND2	ASN- 202	2.92	152.28	H-Bond (Protein Donor)	false
N4	OD1	ASP- 230	3.42	125.88	H-Bond (Ligand Donor)	false
N4	OD2	ASP- 230	2.68	173.82	H-Bond (Ligand Donor)	false
C7	CG	PRO- 232	3.57	0	Hydrophobic	false
C2	CG	PRO- 232	3.86	0	Hydrophobic	false
C7	CE1	TYR- 233	4.26	0	Hydrophobic	false
O49	OG	SER- 260	2.71	166.12	H-Bond (Protein Donor)	false
O48	CZ	ARG- 270	3.88	0	Ionic (Protein Cationic)	false
O50	CZ	ARG- 270	3.59	0	Ionic (Protein Cationic)	false
O48	NH1	ARG- 270	3.06	164.9	H-Bond (Protein Donor)	false
O50	NH2	ARG- 270	2.66	172.18	H-Bond (Protein Donor)	false
C15	CG	GLN- 289	4.03	0	Hydrophobic	false
C12	CD1	LEU- 293	4.31	0	Hydrophobic	false
C24	CD1	LEU- 293	4.07	0	Hydrophobic	false
C14	CD2	LEU- 293	3.66	0	Hydrophobic	false
O9	NH1	ARG- 399	3.33	142.73	H-Bond (Protein Donor)	false
O31	NH2	ARG- 399	2.7	166.84	H-Bond (Protein Donor)	false